从豆豉中分离得到的一株新的耐碱性蛋白酶产生菌——芽孢杆菌 ZJ1502 的发酵条件优化及酶学性质研究
Purification and characterization of a HO-tolerant alkaline protease from Bacillus sp. ZJ1502, a newly isolated strain from fermented bean curd.
机构信息
College of Food Science and Biotechnology, Zhejiang Gongshang University, 149 Jiaogong Road, Hangzhou 310035, Zhejiang Province, People's Republic of China.
College of Food Science and Biotechnology, Zhejiang Gongshang University, 149 Jiaogong Road, Hangzhou 310035, Zhejiang Province, People's Republic of China.
出版信息
Food Chem. 2019 Feb 15;274:510-517. doi: 10.1016/j.foodchem.2018.09.013. Epub 2018 Sep 3.
Alkaline protease was purified from Bacillus sp. ZJ1502 isolated from fermented bean curd and its enzymatic properties were investigated. The final purification fold and specific activity were 18.6 and 30,230 U/mg, respectively. The molecular weight was 14 kDa by SDS-PAGE. The optimal pH and temperature were 10.0 and 40 °C, respectively. Alkaline protease showed high stability at pH 9-11. Mn and Tween-80 improved its activity by 22% and 31%, respectively, while SDS, CMC and EDTA respectively inhibited its activity by 33%, 47% and 22%. Alkaline protease exhibited poor tolerance to n-butyl alcohol and ethanol, but showed resistance to HO. 29.8% of the original activity was still retained after 0.5 M HO treatment for 3 min. The K and V values of this enzyme towards casein were 16.7 mg/ml and 14.7 µg/(min·ml), respectively. This study provides a basis for understanding enzymatic properties of Bacillus sp. ZJ1502 alkaline protease.
碱性蛋白酶从豆豉中分离的芽孢杆菌 ZJ1502 中纯化出来，并对其酶学性质进行了研究。最终的纯化倍数和比活分别为 18.6 和 30,230 U/mg。SDS-PAGE 显示其分子量为 14 kDa。该酶的最适 pH 和温度分别为 10.0 和 40°C。碱性蛋白酶在 pH 9-11 时具有较高的稳定性。Mn 和 Tween-80 分别提高了酶活性 22%和 31%，而 SDS、CMC 和 EDTA 则分别抑制了酶活性 33%、47%和 22%。碱性蛋白酶对正丁醇和乙醇的耐受性较差，但对 HO.29 具有抗性。经 0.5 M HO 处理 3 分钟后，仍保留原酶活的 29.8%。该酶对酪蛋白的 K 和 V 值分别为 16.7 mg/ml 和 14.7 µg/(min·ml)。本研究为了解芽孢杆菌 ZJ1502 碱性蛋白酶的酶学性质提供了依据。
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